PDLI4_BOVIN
ID PDLI4_BOVIN Reviewed; 331 AA.
AC Q3T005;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=PDZ and LIM domain protein 4;
GN Name=PDLIM4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Suppresses SRC activation by recognizing and binding to
CC active SRC and facilitating PTPN13-mediated dephosphorylation of SRC
CC 'Tyr-419' leading to its inactivation. Inactivated SRC dissociates from
CC this protein allowing the initiation of a new SRC inactivation cycle.
CC Involved in reorganization of the actin cytoskeleton (By similarity).
CC In nonmuscle cells, binds to ACTN1 (alpha-actinin-1), increases the
CC affinity of ACTN1 to F-actin (filamentous actin), and promotes
CC formation of actin stress fibers. Involved in regulation of the
CC synaptic AMPA receptor transport in dendritic spines of hippocampal
CC pyramidal neurons directing the receptors toward an insertion at the
CC postsynaptic membrane. Links endosomal surface-internalized GRIA1-
CC containing AMPA receptors to the alpha-actinin/actin cytoskeleton.
CC Increases AMPA receptor-mediated excitatory postsynaptic currents in
CC neurons (By similarity). {ECO:0000250|UniProtKB:P36202,
CC ECO:0000250|UniProtKB:P50479}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via C-terminus only or
CC via combined C-terminus and LIM domain, but not LIM domain only) with
CC PTPN13 (via the second or fourth PDZ domains). Found in a complex with
CC PTPN13 and TRIP6 (By similarity). Interacts (via PDZ domain) with ACTN1
CC and ACTN2 (via C-terminal SDL residues) (By similarity). Interacts (via
CC PDZ domain) with TRIP6 (via the second LIM domain or via the third LIM
CC domain plus C-terminus) (By similarity). Interacts (via LIM domain)
CC with GRIA1 (via C-terminus); this interaction as well as the
CC interaction with alpha-actinin is required for their colocalization in
CC early endosomes. Interacts with PDLIM1 (By similarity). Forms (via LIM
CC domain) a heterodimer with PDLIM3 (By similarity). Interacts directly
CC with SRC (via kinase domain and to a lesser extent the SH2 domain) (By
CC similarity). {ECO:0000250|UniProtKB:P36202,
CC ECO:0000250|UniProtKB:P70271}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P36202}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P36202}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P36202}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P36202}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P36202}; Peripheral membrane protein;
CC Cytoplasmic side {ECO:0000250|UniProtKB:P36202}. Nucleus
CC {ECO:0000250|UniProtKB:P50479}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P50479}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P50479}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P36202}. Note=Localizes to actin stress fibers
CC in nonmuscle cells. Colocalizes with GRIA1 in early endosomes. Enriched
CC in numerous but not all spine-like structures along dendritic branches.
CC Colocalizes with actin and enriched at sites containing larger amounts
CC of actin and alpha-actinin. Targeted efficiently to spines via its PDZ
CC domain-mediated interaction with the alpha-actinin/actin cytoskeletal
CC complex. Localizes to synaptosomes in brain (By similarity).
CC Colocalizes with F-actin. Colocalizes with TRIP6 at cell-cell contacts
CC and lamellipodia. In the cytoplasm, displays a fibrillar pattern with
CC characteristic thick fibers and occasional clusters. Colocalizes with
CC the actin stress fibers. Oxidative stress induces redistribution from
CC cytoskeleton to cytosol. Colocalizes with SRC at the perinuclear
CC region, but not at focal adhesions (By similarity).
CC {ECO:0000250|UniProtKB:P36202, ECO:0000250|UniProtKB:P50479}.
CC -!- PTM: Phosphorylated on tyrosine residue(s). Can be dephosphorylated by
CC PTPN13 (By similarity). {ECO:0000250|UniProtKB:P70271}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102621; AAI02622.1; -; mRNA.
DR RefSeq; NP_001029663.1; NM_001034491.2.
DR AlphaFoldDB; Q3T005; -.
DR SMR; Q3T005; -.
DR STRING; 9913.ENSBTAP00000055868; -.
DR Ensembl; ENSBTAT00000020501; ENSBTAP00000020501; ENSBTAG00000015426.
DR GeneID; 515410; -.
DR KEGG; bta:515410; -.
DR CTD; 8572; -.
DR VEuPathDB; HostDB:ENSBTAG00000015426; -.
DR VGNC; VGNC:32710; PDLIM4.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000159536; -.
DR InParanoid; Q3T005; -.
DR OMA; QYNNPTR; -.
DR OrthoDB; 391515at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000015426; Expressed in prostate gland and 103 other tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0031905; C:early endosome lumen; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0034777; C:recycling endosome lumen; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051393; F:alpha-actinin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Cytoskeleton; Endosome; LIM domain; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Synapse;
KW Synaptosome; Zinc.
FT CHAIN 1..331
FT /note="PDZ and LIM domain protein 4"
FT /id="PRO_0000284656"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 254..313
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50479"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70271"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70271"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36202"
SQ SEQUENCE 331 AA; 35425 MW; CCCCA9494B0DB9C0 CRC64;
MPHSVTLRGP SPWGFRLVGG RDFSVPLTIS RVHAGSKAAL AALCPGDLIQ AINGESTELM
THLEAQNRIK GCRDHLTLSV SRPEGRSWPS TPEDNKAQAH RIHIDSEAQD GSPLTSRRPS
ATGLGPEDGR PGLGSPYGQS PRLPVPHNGS NSEATLLAQM GALHVSPPHS TDPARGLPRS
RDCGVDLGSE VYRMLREPAE PAAAEPKQSG SFRYLQGMLE AGEGGERPGP GGPRNLKPTA
SKLGAPLSGL QGLPECTRCG HGIVGTIVKA RDKLYHPECF MCSDCGLNLK QRGYFFLDER
LYCESHAKAR VKPPEGYDVV AVYPNAKVEL V
